KDM2B_HUMAN - dbPTM
KDM2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM2B_HUMAN
UniProt AC Q8NHM5
Protein Name Lysine-specific demethylase 2B
Gene Name KDM2B
Organism Homo sapiens (Human).
Sequence Length 1336
Subcellular Localization Nucleus, nucleolus .
Protein Description Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex..
Protein Sequence MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQRPIDRQRYDENEDLSDVEEIVSVRGFSLEEKLRSQLYQGDFVHAMEGKDFNYEYVQREALRVPLIFREKDGLGIKMPDPDFTVRDVKLLVGSRRLVDVMDVNTQKGTEMSMSQFVRYYETPEAQRDKLYNVISLEFSHTKLEHLVKRPTVVDLVDWVDNMWPQHLKEKQTEATNAIAEMKYPKVKKYCLMSVKGCFTDFHIDFGGTSVWYHVFRGGKIFWLIPPTLHNLALYEEWVLSGKQSDIFLGDRVERCQRIELKQGYTFFIPSGWIHAVYTPVDSLVFGGNILHSFNVPMQLRIYEIEDRTRVQPKFRYPFYYEMCWYVLERYVYCVTQRSHLTQEYQRESMLIDAPRKPSIDGFSSDSWLEMEEEACDQQPQEEEEKDEEGEGRDRAPKPPTDGSTSPTSTPSEDQEALGKKPKAPALRFLKRTLSNESEESVKSTTLAVDYPKTPTGSPATEVSAKWTHLTEFELKGLKALVEKLESLPENKKCVPEGIEDPQALLEGVKNVLKEHADDDPSLAITGVPVVTWPKKTPKNRAVGRPKGKLGPASAVKLAANRTTAGARRRRTRCRKCEACLRTECGECHFCKDMKKFGGPGRMKQSCIMRQCIAPVLPHTAVCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKIKESEGVVNDELPNCWECPKCNHAGKTGKQKRGPGFKYASNLPGSLLKEQKMNRDNKEGQEPAKRRSECEEAPRRRSDEHSKKVPPDGLLRRKSDDVHLRKKRKYEKPQELSGRKRASSLQTSPGSSSHLSPRPPLGSSLSPWWRSSLTYFQQQLKPGKEDKLFRKKRRSWKNAEDRMALANKPLRRFKQEPEDELPEAPPKTRESDHSRSSSPTAGPSTEGAEGPEEKKKVKMRRKRRLPNKELSRELSKELNHEIQRTENSLANENQQPIKSEPESEGEEPKRPPGICERPHRFSKGLNGTPRELRHQLGPSLRSPPRVISRPPPSVSPPKCIQMERHVIRPPPISPPPDSLPLDDGAAHVMHREVWMAVFSYLSHQDLCVCMRVCRTWNRWCCDKRLWTRIDLNHCKSITPLMLSGIIRRQPVSLDLSWTNISKKQLSWLINRLPGLRDLVLSGCSWIAVSALCSSSCPLLRTLDVQWVEGLKDAQMRDLLSPPTDNRPGQMDNRSKLRNIVELRLAGLDITDASLRLIIRHMPLLSKLHLSYCNHVTDQSINLLTAVGTTTRDSLTEINLSDCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSVSVQFGQVEEKLLQKLS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
26 (in isoform 4)Phosphorylation-51.7025849741
50PhosphorylationRPIDRQRYDENEDLS
CCCCHHHCCCCCCCC
21.1925850435
57PhosphorylationYDENEDLSDVEEIVS
CCCCCCCCCHHHHHH
52.5119664994
64PhosphorylationSDVEEIVSVRGFSLE
CCHHHHHHHCCCCHH
16.2624719451
69PhosphorylationIVSVRGFSLEEKLRS
HHHHCCCCHHHHHHH
37.3826074081
73UbiquitinationRGFSLEEKLRSQLYQ
CCCCHHHHHHHHHHC
39.56-
76PhosphorylationSLEEKLRSQLYQGDF
CHHHHHHHHHHCCCC
34.6726074081
79PhosphorylationEKLRSQLYQGDFVHA
HHHHHHHHCCCCHHH
11.6526074081
94PhosphorylationMEGKDFNYEYVQREA
CCCCCCCHHHHHHHH
14.5028796482
111UbiquitinationVPLIFREKDGLGIKM
CCEEEECCCCCCCCC
53.49-
117UbiquitinationEKDGLGIKMPDPDFT
CCCCCCCCCCCCCCC
42.45-
124PhosphorylationKMPDPDFTVRDVKLL
CCCCCCCCHHHHHHH
23.2423403867
129UbiquitinationDFTVRDVKLLVGSRR
CCCHHHHHHHCCCEE
40.15-
134PhosphorylationDVKLLVGSRRLVDVM
HHHHHCCCEEEEEEE
13.5222817900
145PhosphorylationVDVMDVNTQKGTEMS
EEEEECCCCCCCEEC
31.3522817900
147UbiquitinationVMDVNTQKGTEMSMS
EEECCCCCCCEECHH
66.80-
149PhosphorylationDVNTQKGTEMSMSQF
ECCCCCCCEECHHHH
35.23-
175PhosphorylationDKLYNVISLEFSHTK
HHHHEEEEEECCCHH
19.9829978859
179PhosphorylationNVISLEFSHTKLEHL
EEEEEECCCHHHHHH
22.3729978859
181PhosphorylationISLEFSHTKLEHLVK
EEEECCCHHHHHHHC
35.8129978859
192 (in isoform 4)Phosphorylation-3.32-
210UbiquitinationWPQHLKEKQTEATNA
CHHHHHHHHHHHHHH
62.02-
212PhosphorylationQHLKEKQTEATNAIA
HHHHHHHHHHHHHHH
38.3624719451
215PhosphorylationKEKQTEATNAIAEMK
HHHHHHHHHHHHHCC
20.9621406692
222UbiquitinationTNAIAEMKYPKVKKY
HHHHHHCCCHHHHHE
50.32-
223PhosphorylationNAIAEMKYPKVKKYC
HHHHHCCCHHHHHEE
13.6320068231
229PhosphorylationKYPKVKKYCLMSVKG
CCHHHHHEEEEECCC
5.77-
233PhosphorylationVKKYCLMSVKGCFTD
HHHEEEEECCCCEEE
14.0224719451
248PhosphorylationFHIDFGGTSVWYHVF
EEEECCCCEEEEEEE
22.0824114839
249PhosphorylationHIDFGGTSVWYHVFR
EEECCCCEEEEEEEC
17.5824114839
412 (in isoform 4)Phosphorylation-49.97-
413 (in isoform 4)Phosphorylation-41.09-
414 (in isoform 4)Phosphorylation-12.88-
440PhosphorylationDRAPKPPTDGSTSPT
CCCCCCCCCCCCCCC
62.6122167270
443PhosphorylationPKPPTDGSTSPTSTP
CCCCCCCCCCCCCCC
28.6422167270
443 (in isoform 4)Phosphorylation-28.64-
444PhosphorylationKPPTDGSTSPTSTPS
CCCCCCCCCCCCCCC
44.2322167270
445PhosphorylationPPTDGSTSPTSTPSE
CCCCCCCCCCCCCCH
28.0723401153
447PhosphorylationTDGSTSPTSTPSEDQ
CCCCCCCCCCCCHHH
45.0322167270
448PhosphorylationDGSTSPTSTPSEDQE
CCCCCCCCCCCHHHH
41.5322167270
449PhosphorylationGSTSPTSTPSEDQEA
CCCCCCCCCCHHHHH
33.0622167270
451PhosphorylationTSPTSTPSEDQEALG
CCCCCCCCHHHHHHC
54.6223927012
466 (in isoform 4)Phosphorylation-3.76-
472PhosphorylationALRFLKRTLSNESEE
HHHHHHHHCCCCCHH
32.7123927012
474PhosphorylationRFLKRTLSNESEESV
HHHHHHCCCCCHHHH
37.6323401153
477PhosphorylationKRTLSNESEESVKST
HHHCCCCCHHHHHHC
51.4120164059
480PhosphorylationLSNESEESVKSTTLA
CCCCCHHHHHHCEEE
30.6920164059
483PhosphorylationESEESVKSTTLAVDY
CCHHHHHHCEEEEEC
25.1928450419
484PhosphorylationSEESVKSTTLAVDYP
CHHHHHHCEEEEECC
21.8028450419
485PhosphorylationEESVKSTTLAVDYPK
HHHHHHCEEEEECCC
21.5821815630
490PhosphorylationSTTLAVDYPKTPTGS
HCEEEEECCCCCCCC
10.4630108239
493PhosphorylationLAVDYPKTPTGSPAT
EEEECCCCCCCCCCC
22.9030278072
495PhosphorylationVDYPKTPTGSPATEV
EECCCCCCCCCCCCC
56.3729255136
497PhosphorylationYPKTPTGSPATEVSA
CCCCCCCCCCCCCCC
17.5329255136
500PhosphorylationTPTGSPATEVSAKWT
CCCCCCCCCCCCCCC
40.0629255136
503PhosphorylationGSPATEVSAKWTHLT
CCCCCCCCCCCCCCC
20.2121712546
515UbiquitinationHLTEFELKGLKALVE
CCCHHHHHHHHHHHH
55.81-
532UbiquitinationESLPENKKCVPEGIE
HCCCCCCCCCCCCCC
52.63-
588AcetylationAVGRPKGKLGPASAV
CCCCCCCCCCHHHHH
57.2925953088
593PhosphorylationKGKLGPASAVKLAAN
CCCCCHHHHHHHHHC
36.4125159151
596AcetylationLGPASAVKLAANRTT
CCHHHHHHHHHCCCC
31.9325953088
602PhosphorylationVKLAANRTTAGARRR
HHHHHCCCCHHHHHH
22.3223312004
603PhosphorylationKLAANRTTAGARRRR
HHHHCCCCHHHHHHH
21.6223312004
739PhosphorylationKRGPGFKYASNLPGS
CCCCCCCCCCCCCHH
17.0122817900
741PhosphorylationGPGFKYASNLPGSLL
CCCCCCCCCCCHHHH
35.4922199227
746PhosphorylationYASNLPGSLLKEQKM
CCCCCCHHHHHHHHC
28.7022199227
758AcetylationQKMNRDNKEGQEPAK
HHCCCCCCCCCCCHH
68.4620167786
765AcetylationKEGQEPAKRRSECEE
CCCCCCHHHHHHHHH
60.0920167786
768PhosphorylationQEPAKRRSECEEAPR
CCCHHHHHHHHHCCC
51.1130576142
795PhosphorylationDGLLRRKSDDVHLRK
CCHHCCCCCCCHHHH
36.9125159151
813PhosphorylationYEKPQELSGRKRASS
CCCCHHHCCCCCCCC
35.4824719451
819PhosphorylationLSGRKRASSLQTSPG
HCCCCCCCCCCCCCC
35.3030108239
820PhosphorylationSGRKRASSLQTSPGS
CCCCCCCCCCCCCCC
24.4228464451
823PhosphorylationKRASSLQTSPGSSSH
CCCCCCCCCCCCCCC
42.0321712546
824PhosphorylationRASSLQTSPGSSSHL
CCCCCCCCCCCCCCC
17.8228152594
827PhosphorylationSLQTSPGSSSHLSPR
CCCCCCCCCCCCCCC
31.8628152594
828PhosphorylationLQTSPGSSSHLSPRP
CCCCCCCCCCCCCCC
27.9128152594
829PhosphorylationQTSPGSSSHLSPRPP
CCCCCCCCCCCCCCC
30.0930108239
832PhosphorylationPGSSSHLSPRPPLGS
CCCCCCCCCCCCCCC
17.2818669648
839PhosphorylationSPRPPLGSSLSPWWR
CCCCCCCCCCCHHHH
35.4720873877
840PhosphorylationPRPPLGSSLSPWWRS
CCCCCCCCCCHHHHH
30.9420873877
842PhosphorylationPPLGSSLSPWWRSSL
CCCCCCCCHHHHHHH
22.0318669648
843 (in isoform 4)Phosphorylation-39.69-
844 (in isoform 4)Phosphorylation-10.35-
845 (in isoform 4)Phosphorylation-8.15-
847PhosphorylationSLSPWWRSSLTYFQQ
CCCHHHHHHHHHHHH
18.9123401153
847 (in isoform 4)Phosphorylation-18.91-
848PhosphorylationLSPWWRSSLTYFQQQ
CCHHHHHHHHHHHHH
19.0225159151
850PhosphorylationPWWRSSLTYFQQQLK
HHHHHHHHHHHHHCC
25.0027251275
857SumoylationTYFQQQLKPGKEDKL
HHHHHHCCCCCCHHH
47.5928112733
860AcetylationQQQLKPGKEDKLFRK
HHHCCCCCCHHHHHH
71.8625953088
884AcetylationDRMALANKPLRRFKQ
HHHHHCCCHHHHHHC
39.5626051181
884UbiquitinationDRMALANKPLRRFKQ
HHHHHCCCHHHHHHC
39.56-
890SumoylationNKPLRRFKQEPEDEL
CCHHHHHHCCCCCCC
52.52-
890MethylationNKPLRRFKQEPEDEL
CCHHHHHHCCCCCCC
52.52-
890SumoylationNKPLRRFKQEPEDEL
CCHHHHHHCCCCCCC
52.5228112733
904PhosphorylationLPEAPPKTRESDHSR
CCCCCCCCCCCCCCC
45.5030576142
906 (in isoform 4)Phosphorylation-66.79-
907PhosphorylationAPPKTRESDHSRSSS
CCCCCCCCCCCCCCC
37.0128450419
910PhosphorylationKTRESDHSRSSSPTA
CCCCCCCCCCCCCCC
38.5630576142
910 (in isoform 4)Phosphorylation-38.56-
912PhosphorylationRESDHSRSSSPTAGP
CCCCCCCCCCCCCCC
37.8829255136
913PhosphorylationESDHSRSSSPTAGPS
CCCCCCCCCCCCCCC
38.9529255136
914PhosphorylationSDHSRSSSPTAGPST
CCCCCCCCCCCCCCC
27.7619664994
916PhosphorylationHSRSSSPTAGPSTEG
CCCCCCCCCCCCCCC
46.3129255136
920PhosphorylationSSPTAGPSTEGAEGP
CCCCCCCCCCCCCCH
37.8722115753
921PhosphorylationSPTAGPSTEGAEGPE
CCCCCCCCCCCCCHH
41.3922115753
947PhosphorylationRLPNKELSRELSKEL
CCCCHHHHHHHHHHH
25.4620873877
951PhosphorylationKELSRELSKELNHEI
HHHHHHHHHHHHHHH
21.2323401153
960 (in isoform 4)Phosphorylation-50.06-
961PhosphorylationLNHEIQRTENSLANE
HHHHHHHHHHHHCCC
24.1228450419
962 (in isoform 4)Phosphorylation-47.19-
964PhosphorylationEIQRTENSLANENQQ
HHHHHHHHHCCCCCC
23.7228450419
975PhosphorylationENQQPIKSEPESEGE
CCCCCCCCCCCCCCC
60.1325159151
979PhosphorylationPIKSEPESEGEEPKR
CCCCCCCCCCCCCCC
62.7125159151
1015PhosphorylationLRHQLGPSLRSPPRV
HHHHHCCCCCCCCCC
34.3223898821
1018PhosphorylationQLGPSLRSPPRVISR
HHCCCCCCCCCCCCC
44.5425159151
1024PhosphorylationRSPPRVISRPPPSVS
CCCCCCCCCCCCCCC
35.5623927012
1029PhosphorylationVISRPPPSVSPPKCI
CCCCCCCCCCCCCCE
40.7930266825
1031PhosphorylationSRPPPSVSPPKCIQM
CCCCCCCCCCCCEEE
39.5629255136
1049PhosphorylationVIRPPPISPPPDSLP
ECCCCCCCCCCCCCC
36.8130576142
1054PhosphorylationPISPPPDSLPLDDGA
CCCCCCCCCCCCCCC
37.3529978859
1111UbiquitinationRIDLNHCKSITPLML
EECHHHCCCCCHHHH
37.02-
1142PhosphorylationNISKKQLSWLINRLP
CCCHHHHHHHHHHCC
19.8325247763
1187UbiquitinationVQWVEGLKDAQMRDL
HHHHCCCCCHHHHHH
62.97-
1196PhosphorylationAQMRDLLSPPTDNRP
HHHHHHCCCCCCCCC
35.8129414761
1231MethylationDITDASLRLIIRHMP
CCCHHHHHHHHHHHH
22.73-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of KDM2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM2B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KDM2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP1_HUMANSKP1physical
16943429
BCOR_HUMANBCORphysical
16943429
EZH2_HUMANEZH2physical
19202064
JUN_HUMANJUNphysical
17704768
CUL1_HUMANCUL1physical
17704768
SKP1_HUMANSKP1physical
17704768
SIN3A_HUMANSIN3Aphysical
17704768
H31_HUMANHIST1H3Aphysical
22825849
KDM2B_HUMANKDM2Bphysical
22825849
UB2D1_HUMANUBE2D1physical
22825849
RING2_HUMANRNF2physical
23395003
PCGF1_HUMANPCGF1physical
23395003
RYBP_HUMANRYBPphysical
23395003
RING2_HUMANRNF2physical
25533466
SKP1_HUMANSKP1physical
25533466
BCOR_HUMANBCORphysical
25533466
PCGF1_HUMANPCGF1physical
25533466
GCP60_HUMANACBD3physical
26344197
SKP1_HUMANSKP1physical
17463251
CUL1_HUMANCUL1physical
26725323
RBX1_HUMANRBX1physical
26725323
SKP1_HUMANSKP1physical
26725323
FOS_HUMANFOSphysical
26725323
SKP1_HUMANSKP1physical
28614300

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KDM2B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; THR-493; SER-975AND SER-979, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND SER-497, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND MASSSPECTROMETRY.

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